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Can J Chem 55:3364–3367Īkashi H, Gojobori T (2002) Metabolic efficiency and amino acid composition in the proteomes of Escherichia coli and Bacillus subtilis. These results suggest that the energetic cost of synthesis is not an important selection pressure to incorporate α-amino acids into biological systems.Īhluwalia JC, Ostiguy C, Perron G, Desnoyers JE (1977) Volumes and heat capacities of some amino acids in water at 25 ☌. In acidic and alkaline pH, the non-α-amino acids are thermodynamically more stable than the corresponding α-ones over a broad temperature range. Comparison of their ∆G o values with those of α-amino acids having the same molecular formula showed that the non-α-amino acids have similar ∆G o values to the corresponding α-amino acids in physiologically relevant conditions (neutral pH, <100 ☌). The obtained dataset was then used to calculate the standard molal Gibbs energies ( ∆G o) of the non-α-amino acids as a function of temperature and pH. Temperature dependences of their heat capacities were described based on the revised Helgeson–Kirkham–Flowers (HKF) equations of state. Why does life use α-amino acids exclusively as building blocks of proteins? To address that fundamental question from an energetic perspective, this study estimated the standard molal thermodynamic data for three non-α-amino acids (β-alanine, γ-aminobutyric acid, and ε-aminocaproic acid) and α-amino- n-butyric acid in their zwitterionic, negative, and positive ionization states based on the corresponding experimental measurements reported in the literature.